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Literature summary for 3.4.21.64 extracted from

  • Gheczy, N.; Kuechler, A.; Walde, P.
    Proteinase K activity determination with beta-galactosidase as sensitive macromolecular substrate (2016), Anal. Biochem., 513, 54-60 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information immobilization of the enzyme proK. Compared to free proK, immobilized proK is much less efficient in inactivating beta-galactosidase, most likely due to a decreased mobility of immobilized proK and a restricted accessibility of the substrate to the active site of proK Parengyodontium album

Inhibitors

Inhibitors Comment Organism Structure
PMSF irreversible, covalent proK inhibitor Parengyodontium album

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information enzyme kinetics, overview Parengyodontium album

Organism

Organism UniProt Comment Textmining
Parengyodontium album P06873 i.e. Tritirachium album or Engyodontium album
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation recombinant enzyme expressed from Pichia pastoris Parengyodontium album
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-galactosidase + H2O proteinase K activity determination with beta-galactosidase as sensitive macromolecular substrate, comparison of the native protein-attacking ability of free and immobilized proK, method evaluation, overview. beta-Galactosidase is inactivated by proK. Compared to free proK, immobilized proK is much less efficient in inactivating beta-galactosidase, most likely due to a decreased mobility of immobilized proK and a restricted accessibility of the substrate to the active site of proK Parengyodontium album ?
-
?
additional information beta-galactosidase activity is measured spectrophotometrically with 2-nitrophenyl-beta-galactopyranoside. Hen egg lysozyme, horseradish peroxidase, or Aspergillus sp. glucose oxidase are not inactivated by proteinase K Parengyodontium album ?
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?
succinyl-AAPF-4-nitroanilide + H2O
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Parengyodontium album succinyl-AAPF + 4-nitroaniline
-
?

Synonyms

Synonyms Comment Organism
PROK
-
Parengyodontium album

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
23
-
recombinant enzyme Parengyodontium album

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
recombinant enzyme Parengyodontium album